Hydrodynamic studies on the streptokinase complexes of human plasminogen, Val442-plasminogen, plasmin, and the plasmin-derived light (B) chain
- 1 May 1984
- journal article
- research article
- Published by American Chemical Society (ACS) in Biochemistry
- Vol. 23 (11), 2384-2387
- https://doi.org/10.1021/bi00306a010
Abstract
Note: In lieu of an abstract, this is the article's first page.This publication has 9 references indexed in Scilit:
- Molecular weight of undegraded plasma factor VBiochemistry, 1981
- Activation of human neo-plasminogen-Val442 by urokinase and streptokinase and a kinetic characterization of neoplasmin-Val442.Journal of Biological Chemistry, 1980
- Kinetics of activation of human plasminogen by different activator species at pH 7.4 and 37 degrees C.Journal of Biological Chemistry, 1980
- The binding of tranexamic acid to native (Glu) and modified (Lys) human plasminogen and its effect on conformation.Journal of Biological Chemistry, 1979
- Isolation of a human plasmin-derived, functionally active, light (B) chain capable of forming with streptokinase an equimolar light (B) chain-streptokinase complex with plasminogen activator activity.Journal of Biological Chemistry, 1976
- Interaction of streptokinase with plasminogen. Isolation and characterization of a streptokinase degradation product.Journal of Biological Chemistry, 1976
- The Specific Mechanism of Activation of Human Plasminogen to PlasminJournal of Biological Chemistry, 1967
- PEPTIDE CHAINS OF HUMAN PLASMIN - MECHANISM OF ACTIVATION OF HUMAN PLASMINOGEN TO PLASMIN1967
- Interaction of streptokinase and plasminogenBiochemical and Biophysical Research Communications, 1963